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Volumn 95, Issue 1, 2015, Pages 80-100

The Intimin periplasmic domain mediates dimerisation and binding to peptidoglycan

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CHITIN; GENOMIC DNA; INTIMIN; INVASIN; MEMBRANE PROTEIN; PEPTIDOGLYCAN; PERIPLASMIC PROTEIN; VIRULENCE FACTOR; ADHESIN;

EID: 84919339866     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12840     Document Type: Article
Times cited : (32)

References (50)
  • 1
    • 0031793928 scopus 로고    scopus 로고
    • Iterated profile searches with PSI-BLAST - a tool for discovery in protein databases
    • Altschul, S.F., and Koonin, E.V. (1998) Iterated profile searches with PSI-BLAST - a tool for discovery in protein databases. Trends Biochem Sci 23: 444-447.
    • (1998) Trends Biochem Sci , vol.23 , pp. 444-447
    • Altschul, S.F.1    Koonin, E.V.2
  • 2
    • 0034674162 scopus 로고    scopus 로고
    • The structure of a LysM domain from E.coli membrane-bound lytic murein transglycosylase D (MltD)
    • Bateman, A., and Bycroft, M. (2000) The structure of a LysM domain from E.coli membrane-bound lytic murein transglycosylase D (MltD). J Mol Biol 299: 1113-1119.
    • (2000) J Mol Biol , vol.299 , pp. 1113-1119
    • Bateman, A.1    Bycroft, M.2
  • 3
    • 84873799110 scopus 로고
    • Studies on lysogenesis. I. The mode of phage liberation by lysogenic Escherichia coli
    • Bertani, G. (1951) Studies on lysogenesis. I. The mode of phage liberation by lysogenic Escherichia coli. J Bacteriol 62: 293-300.
    • (1951) J Bacteriol , vol.62 , pp. 293-300
    • Bertani, G.1
  • 5
    • 30344465753 scopus 로고    scopus 로고
    • B.subtilis ykuD protein at 2.0 Å resolution: insights into the structure and function of a novel, ubiquitous family of bacterial enzymes
    • Bielnicki, J., Devedjiev, Y., Derewenda, U., Dauter, Z., Joachimiak, A., and Derewenda, Z.S. (2006) B.subtilis ykuD protein at 2.0 Å resolution: insights into the structure and function of a novel, ubiquitous family of bacterial enzymes. Proteins 62: 144-151.
    • (2006) Proteins , vol.62 , pp. 144-151
    • Bielnicki, J.1    Devedjiev, Y.2    Derewenda, U.3    Dauter, Z.4    Joachimiak, A.5    Derewenda, Z.S.6
  • 6
    • 42549103340 scopus 로고    scopus 로고
    • LysM, a widely distributed protein motif for binding to (peptido)glycans
    • Buist, G., Steen, A., Kok, J., and Kuipers, O. (2008) LysM, a widely distributed protein motif for binding to (peptido)glycans. Mol Microbiol 68: 838-847.
    • (2008) Mol Microbiol , vol.68 , pp. 838-847
    • Buist, G.1    Steen, A.2    Kok, J.3    Kuipers, O.4
  • 7
    • 0029561802 scopus 로고
    • A highly efficient procedure for site-specific mutagenesis of full-length plasmids using Vent DNA polymerase
    • Byrappa, S., Gavin, D.K., and Gupta, K.C. (1995) A highly efficient procedure for site-specific mutagenesis of full-length plasmids using Vent DNA polymerase. Genome Res 5: 1-5.
    • (1995) Genome Res , vol.5 , pp. 1-5
    • Byrappa, S.1    Gavin, D.K.2    Gupta, K.C.3
  • 8
    • 2542459428 scopus 로고    scopus 로고
    • A modified osmotic shock for periplasmic release of a recombinant creatinase from Escherichia coli
    • Chen, Y., Chen, L., Chen, S., Chang, M., and Chen, T. (2004) A modified osmotic shock for periplasmic release of a recombinant creatinase from Escherichia coli. Biochem Eng J 19: 211-215.
    • (2004) Biochem Eng J , vol.19 , pp. 211-215
    • Chen, Y.1    Chen, L.2    Chen, S.3    Chang, M.4    Chen, T.5
  • 9
    • 0033105366 scopus 로고    scopus 로고
    • A region of the Yersinia pseudotuberculosis invasin protein enhances integrin-mediated uptake into mammalian cells and promotes self-association
    • Dersch, P., and Isberg, R.R. (1999) A region of the Yersinia pseudotuberculosis invasin protein enhances integrin-mediated uptake into mammalian cells and promotes self-association. EMBO J 18: 1199-1213.
    • (1999) EMBO J , vol.18 , pp. 1199-1213
    • Dersch, P.1    Isberg, R.R.2
  • 10
    • 0034059454 scopus 로고    scopus 로고
    • An immunoglobulin superfamily-like domain unique to the Yersinia pseudotuberculosis invasin protein is required for stimulation of bacterial uptake via integrin receptors
    • Dersch, P., and Isberg, R.R. (2000) An immunoglobulin superfamily-like domain unique to the Yersinia pseudotuberculosis invasin protein is required for stimulation of bacterial uptake via integrin receptors. Infect Immun 68: 2930-2938.
    • (2000) Infect Immun , vol.68 , pp. 2930-2938
    • Dersch, P.1    Isberg, R.R.2
  • 11
    • 0032694547 scopus 로고    scopus 로고
    • An efficient strategy for assignment of cross-peaks in 3D heteronuclear NOESY experiments
    • Diercks, T., Coles, M., and Kessler, H. (1999) An efficient strategy for assignment of cross-peaks in 3D heteronuclear NOESY experiments. J Biomol NMR 15: 177-180.
    • (1999) J Biomol NMR , vol.15 , pp. 177-180
    • Diercks, T.1    Coles, M.2    Kessler, H.3
  • 12
    • 0011919354 scopus 로고
    • Construction of a triple deletion of Penicillin-binding proteins 4, 5 and 6 in Escherichia coli
    • de Pedro, M., Höltje, J.-V., and Löffelhardt, W. (eds). New York and London: Plenum Press
    • Edwards, D., and Donachie, W.D. (1993) Construction of a triple deletion of Penicillin-binding proteins 4, 5 and 6 in Escherichia coli. In Bacterial Growth and Lysis. de Pedro, M., Höltje, J.-V., and Löffelhardt, W. (eds). New York and London: Plenum Press, pp. 369-374.
    • (1993) Bacterial Growth and Lysis , pp. 369-374
    • Edwards, D.1    Donachie, W.D.2
  • 13
    • 84863527277 scopus 로고    scopus 로고
    • Crystal structures of the outer membrane domain of intimin and invasin from enterohemorrhagic E.coli and enteropathogenic Y.pseudotuberculosis
    • Fairman, J.W., Dautin, N., Wojtowicz, D., Liu, W., Noinaj, N., Barnard, T.J., etal. (2012) Crystal structures of the outer membrane domain of intimin and invasin from enterohemorrhagic E.coli and enteropathogenic Y.pseudotuberculosis. Structure 20: 1233-1243.
    • (2012) Structure , vol.20 , pp. 1233-1243
    • Fairman, J.W.1    Dautin, N.2    Wojtowicz, D.3    Liu, W.4    Noinaj, N.5    Barnard, T.J.6
  • 14
    • 10044222704 scopus 로고    scopus 로고
    • CLANS: a Java application for visualizing protein families based on pairwise similarity
    • Frickey, T., and Lupas, A. (2004) CLANS: a Java application for visualizing protein families based on pairwise similarity. Bioinformatics 20: 3702-3704.
    • (2004) Bioinformatics , vol.20 , pp. 3702-3704
    • Frickey, T.1    Lupas, A.2
  • 15
    • 0023765918 scopus 로고
    • Separation and quantification of muropeptides with high-performance liquid chromatography
    • Glauner, B. (1988) Separation and quantification of muropeptides with high-performance liquid chromatography. Anal Biochem 172: 451-464.
    • (1988) Anal Biochem , vol.172 , pp. 451-464
    • Glauner, B.1
  • 16
    • 0033536633 scopus 로고    scopus 로고
    • Crystal structure of invasin: a bacterial integrin-binding protein
    • Hamburger, Z.A., Brown, M.S., Isberg, R.R., and Bjorkman, P.J. (1999) Crystal structure of invasin: a bacterial integrin-binding protein. Science 286: 291-295.
    • (1999) Science , vol.286 , pp. 291-295
    • Hamburger, Z.A.1    Brown, M.S.2    Isberg, R.R.3    Bjorkman, P.J.4
  • 17
    • 0033918093 scopus 로고    scopus 로고
    • Deuterium isotope effects on the central carbon metabolism of Escherichia coli cells grown on a D2O-containing minimal medium
    • Hochuli, M., Szyperski, T., and Wüthrich, K. (2000) Deuterium isotope effects on the central carbon metabolism of Escherichia coli cells grown on a D2O-containing minimal medium. J Biomol NMR 17: 33-42.
    • (2000) J Biomol NMR , vol.17 , pp. 33-42
    • Hochuli, M.1    Szyperski, T.2    Wüthrich, K.3
  • 18
    • 69949141185 scopus 로고    scopus 로고
    • Acid-stress-induced changes in enterohaemorrhagic Escherichia coli O157:H7 virulence
    • House, B., Kus, J.V., Prayitno, N., Mair, R., Que, L., Chingcuanco, F., etal. (2009) Acid-stress-induced changes in enterohaemorrhagic Escherichia coli O157:H7 virulence. Microbiology 155: 2907-2918.
    • (2009) Microbiology , vol.155 , pp. 2907-2918
    • House, B.1    Kus, J.V.2    Prayitno, N.3    Mair, R.4    Que, L.5    Chingcuanco, F.6
  • 19
    • 0029878720 scopus 로고    scopus 로고
    • VMD: visual molecular dynamics
    • 27-28.
    • Humphrey, W., Dalke, A., and Schulten, K. (1996) VMD: visual molecular dynamics. J Mol GrapH 14: 33-38, 27-28.
    • (1996) J Mol GrapH , vol.14 , pp. 33-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 20
    • 2142657817 scopus 로고    scopus 로고
    • A combined transmembrane topology and signal peptide prediction method
    • Käll, L., Krogh, A., and Sonnhammer, E.L. (2004) A combined transmembrane topology and signal peptide prediction method. J Mol Biol 338: 1027-1036.
    • (2004) J Mol Biol , vol.338 , pp. 1027-1036
    • Käll, L.1    Krogh, A.2    Sonnhammer, E.L.3
  • 21
    • 0032918787 scopus 로고    scopus 로고
    • Structure of the cell-adhesion fragment of intimin from enteropathogenic Escherichia coli
    • Kelly, G., Prasannan, S., Daniell, S., Fleming, K., Frankel, G., Dougan, G., etal. (1999) Structure of the cell-adhesion fragment of intimin from enteropathogenic Escherichia coli. Nat Struct Biol 6: 313-318.
    • (1999) Nat Struct Biol , vol.6 , pp. 313-318
    • Kelly, G.1    Prasannan, S.2    Daniell, S.3    Fleming, K.4    Frankel, G.5    Dougan, G.6
  • 22
    • 0023245332 scopus 로고
    • Two distinct transpeptidation reactions during murein synthesis in Escherichia coli
    • Kraus, W., and Höltje, J.V. (1987) Two distinct transpeptidation reactions during murein synthesis in Escherichia coli. J Bacteriol 169: 3099-3103.
    • (1987) J Bacteriol , vol.169 , pp. 3099-3103
    • Kraus, W.1    Höltje, J.V.2
  • 23
    • 29244447181 scopus 로고    scopus 로고
    • Kalign - an accurate and fast multiple sequence alignment algorithm
    • Lassmann, T., and Sonnhammer, E.L.L. (2005) Kalign - an accurate and fast multiple sequence alignment algorithm. BMC Bioinformatics 6: 298.
    • (2005) BMC Bioinformatics , vol.6 , pp. 298
    • Lassmann, T.1    Sonnhammer, E.L.L.2
  • 24
    • 79960150460 scopus 로고    scopus 로고
    • Adhesins of human pathogens from the genus Yersinia
    • Leo, J.C., and Skurnik, M. (2011) Adhesins of human pathogens from the genus Yersinia. Adv Exp Med Biol 715: 1-15.
    • (2011) Adv Exp Med Biol , vol.715 , pp. 1-15
    • Leo, J.C.1    Skurnik, M.2
  • 25
    • 84858226936 scopus 로고    scopus 로고
    • Type V secretion: mechanism(s) of autotransport through the bacterial outer membrane
    • Leo, J.C., Grin, I., and Linke, D. (2012) Type V secretion: mechanism(s) of autotransport through the bacterial outer membrane. Philos Trans R Soc Lond B Biol Sci 367: 1088-1101.
    • (2012) Philos Trans R Soc Lond B Biol Sci , vol.367 , pp. 1088-1101
    • Leo, J.C.1    Grin, I.2    Linke, D.3
  • 26
    • 0025301659 scopus 로고
    • Identification of the integrin binding domain of the Yersinia pseudotuberculosis invasin protein
    • Leong, J.M., Fournier, R.S., and Isberg, R.R. (1990) Identification of the integrin binding domain of the Yersinia pseudotuberculosis invasin protein. EMBO J 9: 1979-1989.
    • (1990) EMBO J , vol.9 , pp. 1979-1989
    • Leong, J.M.1    Fournier, R.S.2    Isberg, R.R.3
  • 27
    • 0039700109 scopus 로고    scopus 로고
    • Simultaneous measurement of 3JHN,Hα and 3JHα,Hβ coupling constants in 13C,15N-labeled proteins
    • Löhr, F., Schmidt, J.M., and Rüterjans, H. (1999) Simultaneous measurement of 3JHN, Hα and 3JHα, Hβ coupling constants in 13C, 15N-labeled proteins. J Am Chem Soc 121: 11821-11826.
    • (1999) J Am Chem Soc , vol.121 , pp. 11821-11826
    • Löhr, F.1    Schmidt, J.M.2    Rüterjans, H.3
  • 28
    • 0034729685 scopus 로고    scopus 로고
    • Crystal structure of enteropathogenic Escherichia coli intimin-receptor complex
    • Luo, Y., Frey, E.A., Pfuetzner, R.A., Creagh, A.L., Knoechel, D.G., Haynes, C.A., etal. (2000) Crystal structure of enteropathogenic Escherichia coli intimin-receptor complex. Nature 405: 1073-1077.
    • (2000) Nature , vol.405 , pp. 1073-1077
    • Luo, Y.1    Frey, E.A.2    Pfuetzner, R.A.3    Creagh, A.L.4    Knoechel, D.G.5    Haynes, C.A.6
  • 30
    • 84890209865 scopus 로고    scopus 로고
    • Structural and functional studies of gpX of Escherichia coli phage P2 reveal a widespread role for LysM domains in the baseplates of contractile-tailed phages
    • Maxwell, K.L., Hassanabad, M.F., Chang, T., Pirani, N., Bona, D., Edwards, A.M., and Davidson, A.R. (2013) Structural and functional studies of gpX of Escherichia coli phage P2 reveal a widespread role for LysM domains in the baseplates of contractile-tailed phages. J Bacteriol 195: 5461-5468.
    • (2013) J Bacteriol , vol.195 , pp. 5461-5468
    • Maxwell, K.L.1    Hassanabad, M.F.2    Chang, T.3    Pirani, N.4    Bona, D.5    Edwards, A.M.6    Davidson, A.R.7
  • 31
    • 84867325507 scopus 로고    scopus 로고
    • Intimin and invasin export their C-terminus to the bacterial cell surface using an inverse mechanism compared to classical autotransport
    • Oberhettinger, P., Schütz, M., Leo, J.C., Heinz, N., Berger, J., Autenrieth, I.B., and Linke, D. (2012) Intimin and invasin export their C-terminus to the bacterial cell surface using an inverse mechanism compared to classical autotransport. PLoS ONE 7: e47069.
    • (2012) PLoS ONE , vol.7 , pp. e47069
    • Oberhettinger, P.1    Schütz, M.2    Leo, J.C.3    Heinz, N.4    Berger, J.5    Autenrieth, I.B.6    Linke, D.7
  • 32
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: discriminating signal peptides from transmembrane regions
    • Petersen, T.N., Brunak, S., von Heijne, G., and Nielsen, H. (2011) SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat Methods 8: 785-786.
    • (2011) Nat Methods , vol.8 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 33
    • 84864413727 scopus 로고    scopus 로고
    • Monitoring lysin motif-ligand interactions via tryptophan analog fluorescence spectroscopy
    • Petrović, D.M., Leenhouts, K., van Roosmalen, M.L., Kleinjan, F., and Broos, J. (2012) Monitoring lysin motif-ligand interactions via tryptophan analog fluorescence spectroscopy. Anal Biochem 428: 111-118.
    • (2012) Anal Biochem , vol.428 , pp. 111-118
    • Petrović, D.M.1    Leenhouts, K.2    van Roosmalen, M.L.3    Kleinjan, F.4    Broos, J.5
  • 34
    • 84857682188 scopus 로고    scopus 로고
    • In vivo-induced InvA-like autotransporters Ifp and InvC of Yersinia pseudotuberculosis promote interactions with intestinal epithelial cells and contribute to virulence
    • Pisano, F., Kochut, A., Uliczka, F., Geyer, R., Stolz, T., Thiermann, T., etal. (2012) In vivo-induced InvA-like autotransporters Ifp and InvC of Yersinia pseudotuberculosis promote interactions with intestinal epithelial cells and contribute to virulence. Infect Immun 80: 1050-1064.
    • (2012) Infect Immun , vol.80 , pp. 1050-1064
    • Pisano, F.1    Kochut, A.2    Uliczka, F.3    Geyer, R.4    Stolz, T.5    Thiermann, T.6
  • 35
    • 77954375639 scopus 로고    scopus 로고
    • Septal and lateral wall localization of PBP5, the major D,D-carboxypeptidase of Escherichia coli, requires substrate recognition and membrane attachment
    • Potluri, L., Karczmarek, A., Verheul, J., Piette, A., Wilkin, J., Werth, N., etal. (2010) Septal and lateral wall localization of PBP5, the major D, D-carboxypeptidase of Escherichia coli, requires substrate recognition and membrane attachment. Mol Microbiol 77: 300-323.
    • (2010) Mol Microbiol , vol.77 , pp. 300-323
    • Potluri, L.1    Karczmarek, A.2    Verheul, J.3    Piette, A.4    Wilkin, J.5    Werth, N.6
  • 36
    • 0028878573 scopus 로고
    • Variability of peptidoglycan structural parameters in gram-negative bacteria
    • Quintela, J.C., Caparrós, M., and de Pedro, M.A. (1995) Variability of peptidoglycan structural parameters in gram-negative bacteria. FEMS Microbiol Lett 125: 95-100.
    • (1995) FEMS Microbiol Lett , vol.125 , pp. 95-100
    • Quintela, J.C.1    Caparrós, M.2    de Pedro, M.A.3
  • 37
    • 79951493901 scopus 로고    scopus 로고
    • LEEways: tales of EPEC, ATEC and EHEC
    • Schmidt, M.A. (2010) LEEways: tales of EPEC, ATEC and EHEC. Cell Microbiol 12: 1544-1552.
    • (2010) Cell Microbiol , vol.12 , pp. 1544-1552
    • Schmidt, M.A.1
  • 38
    • 84863205849 scopus 로고    scopus 로고
    • NIH Image to ImageJ: 25 years of image analysis
    • Schneider, C.A., Rasband, W.S., and Eliceiri, K.W. (2012) NIH Image to ImageJ: 25 years of image analysis. Nat Methods 9: 671-675.
    • (2012) Nat Methods , vol.9 , pp. 671-675
    • Schneider, C.A.1    Rasband, W.S.2    Eliceiri, K.W.3
  • 39
    • 68349093958 scopus 로고    scopus 로고
    • TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
    • Shen, Y., Delaglio, F., Cornilescu, G., and Bax, A. (2009) TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J Biomol NMR 44: 213-223.
    • (2009) J Biomol NMR , vol.44 , pp. 213-223
    • Shen, Y.1    Delaglio, F.2    Cornilescu, G.3    Bax, A.4
  • 40
    • 0021253806 scopus 로고
    • Lack of correlation between the presence of plasmids and fimbriae in Yersinia enterocolitica and Yersinia pseudotuberculosis
    • Skurnik, M. (1984) Lack of correlation between the presence of plasmids and fimbriae in Yersinia enterocolitica and Yersinia pseudotuberculosis. J Appl Bacteriol 56: 355-363.
    • (1984) J Appl Bacteriol , vol.56 , pp. 355-363
    • Skurnik, M.1
  • 41
    • 23144452044 scopus 로고    scopus 로고
    • The HHpred interactive server for protein homology detection and structure prediction
    • Söding, J., Biegert, A., and Lupas, A.N. (2005) The HHpred interactive server for protein homology detection and structure prediction. Nucleic Acids Res 33: W244-W248.
    • (2005) Nucleic Acids Res , vol.33 , pp. W244-W248
    • Söding, J.1    Biegert, A.2    Lupas, A.N.3
  • 42
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier, F.W. (2005) Protein production by auto-induction in high density shaking cultures. Protein Expr Purif 41: 207-234.
    • (2005) Protein Expr Purif , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 43
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G., and Gibson, T.J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 44
    • 0346334430 scopus 로고    scopus 로고
    • Self-association of EPEC intimin mediated by the β-barrel-containing anchor domain: a role in clustering of the Tir receptor
    • Touzé, T., Hayward, R.D., Eswaran, J., Leong, J.M., and Koronakis, V. (2004) Self-association of EPEC intimin mediated by the β-barrel-containing anchor domain: a role in clustering of the Tir receptor. Mol Microbiol 51: 73-87.
    • (2004) Mol Microbiol , vol.51 , pp. 73-87
    • Touzé, T.1    Hayward, R.D.2    Eswaran, J.3    Leong, J.M.4    Koronakis, V.5
  • 45
    • 84934444524 scopus 로고    scopus 로고
    • Expression and purification of soluble His(6)-tagged TEV protease
    • Tropea, J.E., Cherry, S., and Waugh, D.S. (2009) Expression and purification of soluble His(6)-tagged TEV protease. Methods Mol Biol 498: 297-307.
    • (2009) Methods Mol Biol , vol.498 , pp. 297-307
    • Tropea, J.E.1    Cherry, S.2    Waugh, D.S.3
  • 47
    • 78650987801 scopus 로고    scopus 로고
    • The bacterial intimins and invasins: a large and novel family of secreted proteins
    • Tsai, J.C., Yen, M., Castillo, R., Leyton, D.L., Henderson, I.R., and Saier, M.H. (2010) The bacterial intimins and invasins: a large and novel family of secreted proteins. PLoS ONE 5: e14403-e14414.
    • (2010) PLoS ONE , vol.5 , pp. e14403-e14414
    • Tsai, J.C.1    Yen, M.2    Castillo, R.3    Leyton, D.L.4    Henderson, I.R.5    Saier, M.H.6
  • 48
    • 84881330840 scopus 로고    scopus 로고
    • AcmD, a homolog of the major autolysin AcmA of Lactococcus lactis, binds to the cell wall and contributes to cell separation and autolysis
    • Visweswaran, G.R.R., Steen, A., Leenhouts, K., Szeliga, M., Ruban, B., Hesseling-Meinders, A., etal. (2013) AcmD, a homolog of the major autolysin AcmA of Lactococcus lactis, binds to the cell wall and contributes to cell separation and autolysis. PLoS ONE 8: e72167.
    • (2013) PLoS ONE , vol.8 , pp. e72167
    • Visweswaran, G.R.R.1    Steen, A.2    Leenhouts, K.3    Szeliga, M.4    Ruban, B.5    Hesseling-Meinders, A.6
  • 49
    • 0027357769 scopus 로고
    • 3D triple-resonance NMR techniques for the sequential assignment of NH and 15N resonances in 15N- and 13C-labelled proteins
    • Weisemann, R., Rüterjans, H., and Bermel, W. (1993) 3D triple-resonance NMR techniques for the sequential assignment of NH and 15N resonances in 15N- and 13C-labelled proteins. J Biomol NMR 3: 113-120.
    • (1993) J Biomol NMR , vol.3 , pp. 113-120
    • Weisemann, R.1    Rüterjans, H.2    Bermel, W.3
  • 50
    • 34547634728 scopus 로고    scopus 로고
    • pH of the cytoplasm and periplasm of Escherichia coli: rapid measurement by green fluorescent protein fluorimetry
    • Wilks, J.C., and Slonczewski, J.L. (2007) pH of the cytoplasm and periplasm of Escherichia coli: rapid measurement by green fluorescent protein fluorimetry. J Bacteriol 189: 5601-5607.
    • (2007) J Bacteriol , vol.189 , pp. 5601-5607
    • Wilks, J.C.1    Slonczewski, J.L.2


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